C3114
Anti-Calpain-13 (Domain III, N-Terminal), Large Subunit antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
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关于此项目
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA (i), IHC, IP, WB
Citations:
6
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous glycerol solution
species reactivity
rat, human, mouse
concentration
~1 mg/mL
technique(s)
immunohistochemistry: suitable, immunoprecipitation (IP): suitable, indirect ELISA: suitable, western blot: 1:1,000
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Quality Level
Gene Information
human ... CAPN13(92291)
mouse ... Capn13(381122)
rat ... Capn13(362701)
General description
Calpains are calcium-activated, non-lysosomal cysteine proteases that cleave cytoskeletal and submembranous proteins. It is an intracellular cysteine protease that is present in all mammalian tissues. Anti-Calpain-13 (Domain I, N-Terminal), Large Subunit is developed in rabbit using a synthetic peptide corresponding to domain I of the large subunit of human calpain 13 (capn-13) as immunogen. The antibody is affinity purified using agarose to which the immunogen peptide has been bound.
Immunogen
synthetic peptide corresponding to domain III of the large subunit of human calpain 13.
Application
Anti-Calpain-13 is suitable for immunohistochemistry, immunoprecipitation and indirect ELISA. It is also suitable for western blot at a dilution of 1:1,000
Biochem/physiol Actions
Calpains are involved in a variety of processes including cytoskeletal reorganization, muscle protein degradation, cell proliferation, differentiation, and vesicular secretion. Anti-Calpain-13 (Domain I, N-Terminal), Large Subunit recognizes domain I in the large subunit of human calpain 13 by various immunochemical techniques including immunoblotting, immunoprecipitation, immunohistochemistry, and ELISA. It detects human, rat, and mouse calpain 13 and does not crossreact with other calpain family members (calpain 1, calpain 2, calpain 3, etc.). The antibody binds to the reduced and non-reduced protein. By immunoblotting against the reduced protein, the antibody identifies bands at approximately 64 kDa, 52 kDa, 48 kDa, 40 kDa, and aseries of smaller forms.
Physical form
Solution in 0.01 M phosphate buffered saline containing 50% glycerol and 0.05% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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存储类别
10 - Combustible liquids
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此项目有
S S Murray et al.
Experimental cell research, 233(2), 297-309 (1997-06-15)
The calpain-calpastatin system, which consists of calpains I and II (two ubiquitously distributed calcium-activated papain-like cysteine proteases), as well as calpastatin (the endogenous calpain inhibitor), plays an important role in cell proliferation and differentiation in many tissues. However, its contribution
D Stockholm et al.
Experimental cell research, 252(2), 392-400 (1999-10-21)
We have synthesized dextran derivatives called RGTAs (for regenerating agents) that were designed to mimic some of the properties of heparin or heparan sulfate to interact with and protect heparin binding growth factors. Some of these growth factors have been
S Kulkarni et al.
The Journal of biological chemistry, 274(30), 21265-21275 (1999-07-20)
Integrin-induced adhesion leads to cytoskeletal reorganizations, cell migration, spreading, proliferation, and differentiation. The details of the signaling events that induce these changes in cell behavior are not well understood but they appear to involve activation of Rho family members which
D Balcerzak et al.
Journal of cell science, 108 ( Pt 5), 2077-2082 (1995-05-01)
Previous studies have led to the hypothesis of a possible role for m-calpain (EC 3.4.22.17) in myoblast fusion in culture in vitro. To support this hypothesis, an antisense strategy has been used with cultured primary rat myoblasts. Using an appropriate
G V Johnson et al.
BioEssays : news and reviews in molecular, cellular and developmental biology, 19(11), 1011-1018 (1997-12-12)
Calpains are a family of calcium-dependent thiol-proteases which are proposed to be involved in many physiological processes as well as pathological conditions. Calpains are likely to be involved in processing of numerous enzymes and cytoskeletal components, thereby linking their activity
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